ID   GPDQ_ENTLS              Reviewed;         278 AA.
AC   E3GCF1;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   02-SEP-2026, entry version 77.
DE   RecName: Full=Glycerophosphodiester phosphodiesterase GpdQ {ECO:0000250|UniProtKB:Q6XBH1};
DE            Short=GDPD {ECO:0000250|UniProtKB:Q6XBH1};
DE            Short=Glycerophosphoryl diester phosphodiesterase {ECO:0000250|UniProtKB:Q6XBH1};
DE            EC=3.1.4.46 {ECO:0000250|UniProtKB:Q6XBH1};
DE   AltName: Full=Glycerophosphodiesterase {ECO:0000250|UniProtKB:Q6XBH1};
DE   AltName: Full=Glycerophosphorylethanolamine phosphodiesterase {ECO:0000250|UniProtKB:Q6XBH1};
DE            Short=GPE phosphodiesterase {ECO:0000250|UniProtKB:Q6XBH1};
GN   Name=gpdQ {ECO:0000250|UniProtKB:Q6XBH1};
GN   OrderedLocusNames=Entcl_3882;
OS   Enterobacter lignolyticus (strain SCF1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=701347;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCF1;
RX   PubMed=22180812; DOI=10.4056/sigs.2104875;
RA   Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA   Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA   Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT   "Complete genome sequence of 'Enterobacter lignolyticus' SCF1.";
RL   Stand. Genomic Sci. 5:69-85(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the 3'-5' phosphodiester bond of
CC       glycerophosphodiesters such as glycerophosphorylethanolamine (GPE), a
CC       typical phospholipid metabolite. {ECO:0000250|UniProtKB:Q6XBH1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sn-glycero-3-phosphodiester + H2O = an alcohol + sn-glycerol
CC         3-phosphate + H(+); Xref=Rhea:RHEA:12969, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:83408; EC=3.1.4.46;
CC         Evidence={ECO:0000250|UniProtKB:Q6XBH1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sn-glycero-3-phosphoethanolamine + H2O = ethanolamine + sn-
CC         glycerol 3-phosphate + H(+); Xref=Rhea:RHEA:29319, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57597, ChEBI:CHEBI:57603,
CC         ChEBI:CHEBI:143890; Evidence={ECO:0000250|UniProtKB:Q6XBH1};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q6XBH1};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q6XBH1};
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC       III family. {ECO:0000305}.
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DR   EMBL; CP002272; ADO50122.1; -; Genomic_DNA.
DR   RefSeq; WP_013367845.1; NC_014618.1.
DR   AlphaFoldDB; E3GCF1; -.
DR   SMR; E3GCF1; -.
DR   STRING; 701347.Entcl_3882; -.
DR   KEGG; esc:Entcl_3882; -.
DR   eggNOG; COG1409; Bacteria.
DR   HOGENOM; CLU_070320_2_1_6; -.
DR   Proteomes; UP000006872; Chromosome.
DR   GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; ISS:UniProtKB.
DR   CDD; cd07402; MPP_GpdQ; 1.
DR   Gene3D; 3.30.750.180; GpdQ, beta-strand dimerisation domain; 1.
DR   Gene3D; 3.60.21.40; GpdQ, catalytic alpha/beta sandwich domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR050884; CNP_phosphodiesterase-III.
DR   InterPro; IPR026575; GpdQ/CpdA-like.
DR   InterPro; IPR042281; GpdQ_beta-strand.
DR   InterPro; IPR042283; GpdQ_catalytic.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR42988:SF2; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE CBUA0032-RELATED; 1.
DR   PANTHER; PTHR42988; PHOSPHOHYDROLASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Glycerol metabolism; Hydrolase; Iron; Metal-binding; Reference proteome.
FT   CHAIN           1..278
FT                   /note="Glycerophosphodiester phosphodiesterase GpdQ"
FT                   /id="PRO_0000413367"
FT   BINDING         8
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         10
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         50
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         50
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         80
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         156
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         195
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         197
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
SQ   SEQUENCE   278 AA;  31308 MW;  CFF0D7D4DDB3AF10 CRC64;
     MLLAHISDTH FRSQNHKLYG FIDVNAGNAD VVSQLNGLRE RPDAVVVSGD IVNCGRPEEY
     QVARQVLGAL RYPLLLIPGN HDDKACFLEY LRPLCPQLGS DPQNMRYAID DFATRLLFID
     SSLAGHAKGW LTDNTVAWLE AQLSDAGDKP TAVFMHHPPL PLGNAQMDPI ACENGHRLLA
     LVERFPSLVR IFCGHNHNLT MTQYRQATIA TLPATVHQVP YCHEDTRPYY DMSPPSCLMH
     RQVGEQWVSY QHSLAHYAGP WLYDEHISCP TDERRSPC
//